EzCatDB: D00269

DB codeD00269
CATH domainDomain 13.90.1150.10
Domain 23.40.640.10Catalytic domain
E.C.4.4.1.14
CSA1b8g

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00515,M00031,D00279
3.90.1150.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00515,M00031,D00279

Enzyme Name
Swiss-protKEGG

P37821P18485
Protein name1-aminocyclopropane-1-carboxylate synthase1-aminocyclopropane-1-carboxylate synthase 21-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropanecarboxylate synthase
1-aminocyclopropane-1-carboxylic acid synthase
1-aminocyclopropane-1-carboxylate synthetase
aminocyclopropanecarboxylic acid synthase
aminocyclopropanecarboxylate synthase
ACC synthase
S-adenosyl-L-methionine methylthioadenosine-lyase
SynonymsACC synthase
EC 4.4.1.14
S-adenosyl-L-methionine methylthioadenosine-lyase
ACC synthase 2
EC 4.4.1.14
Le-ACS2
ACS-2
S-adenosyl-L-methionine methylthioadenosine-lyase 2

KEGG pathways
MAP codePathways
MAP00271Methionine metabolism

Swiss-prot:Accession NumberP37821P18485
Entry name1A1C_MALDO1A12_SOLLC
ActivityS-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine.S-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine.
SubunitHomodimer.Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure.
Subcellular location

CofactorPyridoxal phosphate.Pyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C00019C01234C00170
CompoundPyridoxal phosphateS-Adenosyl-L-methionine1-Aminocyclopropane-1-carboxylateMethylthioadenosine
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,amine group,nucleoside,sulfonium ionamino acidsamine group,nucleoside,sulfide group
1b8gA01UnboundUnboundUnboundUnboundUnbound
1b8gB01UnboundUnboundUnboundUnboundUnbound
1m7yA01UnboundUnboundUnboundUnboundUnbound
1m4nA01UnboundUnboundUnboundUnboundUnbound
1iaxA01UnboundUnboundUnboundUnboundUnbound
1iaxB01UnboundUnboundUnboundUnboundUnbound
1iayA01UnboundUnboundUnboundUnboundUnbound
1b8gA02Bound:PLPUnboundUnboundUnboundUnbound
1b8gB02Bound:PLPUnboundUnboundUnboundUnbound
1m7yA02Analogue:PPGUnboundUnboundUnboundIntermediate-analogue:PPG
1m4nA02Bound:PLPAnalogue:AADUnboundUnboundIntermediate-analogue:PLP-AAD
1iaxA02Bound:PLPUnboundUnboundUnboundUnbound
1iaxB02Bound:PLPUnboundUnboundUnboundUnbound
1iayA02Bound:PLPUnboundAnalogue:AVGUnboundUnbound

Active-site residues
resource
literature [9] & [11]
pdbCatalytic residuesModified residues
1b8gA01

1b8gB01

1m7yA01

1m4nA01

1iaxA01

1iaxB01

1iayA01

1b8gA02TYR 145;LYS 273
LYS 273(PLP binding)
1b8gB02TYR 145;LYS 273
LYS 273(PLP binding)
1m7yA02TYR 145;LYS 273
LYS 273(PLP binding)
1m4nA02TYR 145;LYS 273
LYS 273(PLP binding)
1iaxA02TYR 152;LYS 278
LYS 278(PLP binding)
1iaxB02TYR 152;LYS 278
LYS 278(PLP binding)
1iayA02TYR 152;LYS 278
LYS 278(PLP binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.4, p.7824
[7]Scheme 4B, Scheme 6, p.15486-15487
[8]p.8
[9]Scheme 2, p.748-7494
[10]Scheme 1, Scheme 3A, p.122833
[11]p.38214, Fig.6, p.382155
[12]Scheme 3, p.3840-3841

references
[1]
PubMed ID3865199
JournalProc Natl Acad Sci U S A
Year1985
Volume82
Pages7820-4
AuthorsRamalingam K, Lee KM, Woodard RW, Bleecker AB, Kende H
TitleStereochemical course of the reaction catalyzed by the pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase.
[2]
PubMed ID2712568
JournalArch Biochem Biophys
Year1989
Volume271
Pages107-12
AuthorsSatoh S, Yang SF
TitleSpecificity of S-adenosyl-L-methionine in the inactivation and the labeling of 1-aminocyclopropane-1-carboxylate synthase isolated from tomato fruits.
[3]
PubMed ID1421146
JournalPlant Mol Biol
Year1992
Volume20
Pages425-36
AuthorsBotella JR, Arteca JM, Schlagnhaufer CD, Arteca RN, Phillips AT
TitleIdentification and characterization of a full-length cDNA encoding for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from etiolated mung bean hypocotyl segments and expression of its mRNA in response to indole-3-acetic acid.
[4]
PubMed ID7966311
JournalJ Mol Biol
Year1994
Volume243
Pages947-9
AuthorsHohenester E, White MF, Kirsch JF, Jansonius JN
TitleCrystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene.
[5]
PubMed ID7809054
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages12428-32
AuthorsWhite MF, Vasquez J, Yang SF, Kirsch JF
TitleExpression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.
[6]
PubMed ID8557119
JournalFEBS Lett
Year1996
Volume378
Pages286-90
AuthorsLi N, Huxtable S, Yang SF, Kung SD
TitleEffects of N-terminal deletions on 1-aminocyclopropane-1-carboxylate synthase activity.
[7]
PubMed ID9398277
JournalBiochemistry
Year1997
Volume36
Pages15477-88
AuthorsLi Y, Feng L, Kirsch JF
TitleKinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase.
[8]
PubMed ID9279127
JournalIndian J Exp Biol
Year1997
Volume35
Pages1-17
AuthorsPenrose DM, Glick BR
TitleEnzymes that regulate ethylene levels--1-aminocyclopropane-1-carboxylic acid (ACC) deaminase, ACC synthase and ACC oxidase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS)
Medline ID20079531
PubMed ID10610793
JournalJ Mol Biol
Year1999
Volume294
Pages745-56
AuthorsCapitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN
TitleStructure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
Related PDB1b8g
Related Swiss-protP37821
[10]
PubMed ID11591146
JournalBiochemistry
Year2001
Volume40
Pages12276-84
AuthorsMcCarthy DL, Capitani G, Feng L, Gruetter MG, Kirsch JF
TitleGlutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.
[11]
CommentsX-ray crystallography
PubMed ID11431475
JournalJ Biol Chem
Year2001
Volume276
Pages38210-6
AuthorsHuai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H
TitleCrystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms.
Related PDB1iax
[12]
PubMed ID11888303
JournalBiochemistry
Year2002
Volume41
Pages3836-42
AuthorsEliot AC, Kirsch JF
TitleModulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.
[13]
PubMed ID12228256
JournalJ Biol Chem
Year2002
Volume277
Pages49735-42
AuthorsCapitani G, McCarthy DL, Gut H, Grutter MG, Kirsch JF
TitleApple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
Related PDB1m7y
[14]
PubMed ID12686108
JournalBiochim Biophys Acta
Year2003
Volume1647
Pages55-60
AuthorsCapitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG
TitleStructure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
Related PDB1m4n

comments
This enzyme catalyzes a PLP-dependent elimination reaction, followed by an isomerization reaction.

createdupdated
2004-05-242009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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